1JAL
YCHF PROTEIN (HI0393)
1JAL の概要
| エントリーDOI | 10.2210/pdb1jal/pdb |
| 分子名称 | YchF protein (2 entities in total) |
| 機能のキーワード | nucleotide-binding fold, structural genomics, structure 2 function project, s2f, unknown function |
| 由来する生物種 | Haemophilus influenzae |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 79588.54 |
| 構造登録者 | Teplyakov, A.,Gilliland, G.L.,Structure 2 Function Project (S2F) (登録日: 2001-05-30, 公開日: 2003-03-25, 最終更新日: 2024-02-07) |
| 主引用文献 | Teplyakov, A.,Gilliland, G.L. Crystal structure of the YchF protein reveals binding sites for GTP and nucleic acid J.BACTERIOL., 185:4031-4037, 2003 Cited by PubMed Abstract: The bacterial protein encoded by the gene ychF is 1 of 11 universally conserved GTPases and the only one whose function is unknown. The crystal structure determination of YchF was sought to help with the functional assignment of the protein. The YchF protein from Haemophilus influenzae was cloned and expressed, and the crystal structure was determined at 2.4 A resolution. The polypeptide chain is folded into three domains. The N-terminal domain has a mononucleotide binding fold typical for the P-loop NTPases. An 80-residue domain next to it has a pronounced alpha-helical coiled coil. The C-terminal domain features a six-stranded half-barrel that curves around an alpha-helix. The crablike three-domain structure of YchF suggests the binding site for a double-stranded nucleic acid in the cleft between the domains. The structure of the putative GTP-binding site is consistent with the postulated guanine specificity of the protein. Fluorescence measurements have demonstrated the ability of YchF to bind a double-stranded nucleic acid and GTP. Taken together with other experimental data and genomic analysis, these results suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translation factor. PubMed: 12837776DOI: 10.1128/JB.185.14.4031-4037.2003 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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